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THE PLANT CELL, Vol 1, Issue 3 373-379, Copyright © 1989 by American Society of Plant Biologists

RESEARCH ARTICLES

Nodule-Specific Kinases Phosphorylating Nuclear Factors in Isolated Nuclei

H. Suzuki and DPS. Verma
Department of Molecular Genetics and The Biotechnology Center, Ohio State University, 1060 Carmack Road, Columbus, Ohio 43210-1002

In vitro phosphorylation of total nuclear proteins from soybean (Glycine max L) nodules formed by Bradyrhizobium japonicum 61A76 showed several differences in comparison with those from uninfected roots or embryonic-axes nuclei. Three types of protein phosphorylations were observed in nodule nuclei: Ca2+- and calmodulin-independent, Ca2+- and calmodulin-dependent, and Ca2+-dependent but calmodulin-independent. In addition, Ca2+-dependent dephosphorylation of some nuclear proteins was observed in nodule nuclei. The first and second types of phosphorylations were also present in root nuclei, but the trifluoperazine-insensitive and Ca2+-dependent phosphorylation (indicating calmodulin independence) occurs only in nodules. The latter appears to phosphorylate a nodule-specific protein of 65 kilodaltons and this protein was purified from other nuclear phosphorylated proteins. In addition, some nuclear proteins from uninfected tissue were found to be phosphorylated or dephosphorylated by kinases or phosphatases that originated from the nodule nuclei. These data suggest that some activities of nuclear factors in nodules may be regulated by specific phosphorylation or dephosphorylation during symbiotic interactions with rhizobia.




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Copyright © 1989 by the American Society of Plant Biologists